(Q27695578)

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Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site

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Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site (English)

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Europe PubMed Central

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1 June 2020

Jean-Marie Wurtz

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1 June 2020

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1 June 2020

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Nathalie Troffer-Charlier

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1 June 2020

Luc Bonnefond

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September 2014

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Acta Crystallographica Section D: Biological Crystallography

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1 June 2020

70

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1 June 2020

Pt 9

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1 June 2020

2401-2412

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1 June 2020

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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Comprehending dynamic protein methylation with mass spectrometry

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Minimal functional sites allow a classification of zinc sites in proteins

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Crystal structure of the human PRMT5:MEP50 complex

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Protein arginine methylation in mammals: who, what, and why

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Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.

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Cloning, expression, purification and preliminary X-ray crystallographic analysis of mouse protein arginine methyltransferase 7.

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A remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine

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21 January 2018

Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats

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Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity

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The testis-specific factor CTCFL cooperates with the protein methyltransferase PRMT7 in H19 imprinting control region methylation

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21 January 2018

Methylation of eukaryotic elongation factor 2 induced by basic fibroblast growth factor via mitogen-activated protein kinase

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Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1

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21 January 2018

Distinct transcriptional outputs associated with mono- and dimethylated histone H3 arginine 2.

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Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively.

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Automated matching of high- and low-resolution structural models

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Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential

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Structural classification of zinc fingers: survey and summary

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Inference of macromolecular assemblies from crystalline state

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A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism

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21 January 2018

PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

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21 January 2018

S-Adenosylmethionine:protein-arginine methyltransferase. Purification and mechanism of the enzyme

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21 January 2018

Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver

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21 January 2018

The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase

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21 January 2018

Crystal Structure of TDRD3 and Methyl-Arginine Binding Characterization of TDRD3, SMN and SPF30

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Analysis Tool Web Services from the EMBL-EBI.

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Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance

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PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity

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Kinetic mechanism of protein arginine methyltransferase 1.

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21 January 2018

Kinetic mechanism of protein arginine methyltransferase 6 (PRMT6).

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21 January 2018

Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis

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New developments in the ATSAS program package for small-angle scattering data analysis

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Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family

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21 January 2018

Mechanistic studies on transcriptional coactivator protein arginine methyltransferase 1.

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Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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